Q9UK32 (KS6A6_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Ribosomal protein S6 kinase alpha-6
Short name=S6K-alpha-6
EC=2.7.11.1

Alternative name(s):
90 kDa ribosomal protein S6 kinase 6
Short name=p90-RSK 6
Short name=p90RSK6
Ribosomal S6 kinase 4
Short name=RSK-4
pp90RSK4

Gene names

Name:	RPS6KA6
Synonyms:	RSK4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	745 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Constitutively active serine/threonine-protein kinase that exhibits growth-factor-independent kinase activity and that may participate in p53/TP53-dependent cell growth arrest signaling and play an inhibitory role during embryogenesis. Ref.6 Ref.7
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Cofactor	Magnesium By similarity.
Enzyme regulation	Constitutively activated by phosphorylation at Ser-232, Ser-372, and Ser-389 in serum-starved cells. Does not require growth factor stimulation for significant kinase activity. Ref.7
Subunit structure	Forms a complex with MAPK3/ERK1 but not with MAPK9 or MAPK14 in serum-starved cells.
Subcellular location	Cytoplasm › cytosol. Nucleus. Note: Predominantly cytosolic. Ref.7
Post-translational modification	Phosphorylated at Ser-232, Ser-372, and Ser-389 in serum-starved cells. Ref.7
Sequence similarities	Belongs to the protein kinase superfamily. AGC Ser/Thr protein kinase family. S6 kinase subfamily. Contains 1 AGC-kinase C-terminal domain. Contains 2 protein kinase domains.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Polymorphism
Domain	Repeat
Ligand	ATP-binding Magnesium Metal-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in transcription of p21 class mediator Inferred from mutant phenotype Ref.6. Source: UniProtKB axon guidance Traceable author statement. Source: Reactome central nervous system development Traceable author statement Ref.1. Source: ProtInc intracellular protein kinase cascade Inferred from electronic annotation. Source: InterPro negative regulation of ERK1 and ERK2 cascade Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of embryonic development Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of mesoderm development Inferred from sequence or structural similarity. Source: UniProtKB synaptic transmission Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion binding Inferred from electronic annotation. Source: InterPro protein kinase activity Traceable author statement Ref.1. Source: ProtInc protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 745	745	Ribosomal protein S6 kinase alpha-6		PRO_0000086209
Regions
	Domain	73 – 330	258	Protein kinase 1
	Domain	331 – 400	70	AGC-kinase C-terminal
	Domain	426 – 683	258	Protein kinase 2
	Nucleotide binding	79 – 87	9	ATP By similarity
	Nucleotide binding	432 – 440	9	ATP By similarity
Sites
	Active site	198	1	Proton acceptor By similarity
	Active site	543	1	Proton acceptor By similarity
	Binding site	105	1	ATP By similarity
	Binding site	455	1	ATP By similarity
Amino acid modifications
	Modified residue	232	1	Phosphoserine Ref.7
	Modified residue	372	1	Phosphoserine Ref.7
	Modified residue	389	1	Phosphoserine Ref.7 Ref.9
Natural variations
	Natural variant	140	1	Y → C in a lung large cell carcinoma sample; somatic mutation. Ref.10		VAR_040637
	Natural variant	258	1	S → T in a lung adenocarcinoma sample; somatic mutation. Ref.10		VAR_040638
	Natural variant	692	1	D → N. Ref.10 Corresponds to variant rs6616890 [ dbSNP | Ensembl ].		VAR_030670
Experimental info
	Mutagenesis	372	1	S → A: No effect on activity. Ref.7
	Mutagenesis	389	1	S → A: Strongly decreases activity. Ref.7
	Mutagenesis	581	1	T → A: No effect on activity. Ref.7
	Sequence conflict	116	1	D → G in CAG38803. Ref.2
	Sequence conflict	295	1	F → L in CAG38803. Ref.2
	Sequence conflict	341	1	R → G in CAG38803. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Q9UK32 [UniParc]. Last modified May 1, 2000. Version 1. Checksum: 5EC5AB2FA1C19DE8	FASTA	745	83,872
	10 20 30 40 50 60 MLPFAPQDEP WDREMEVFSG GGASSGEVNG LKMVDEPMEE GEADSCHDEG VVKEIPITHH 70 80 90 100 110 120 VKEGYEKADP AQFELLKVLG QGSFGKVFLV RKKTGPDAGQ LYAMKVLKKA SLKVRDRVRT 130 140 150 160 170 180 KMERDILVEV NHPFIVKLHY AFQTEGKLYL ILDFLRGGDV FTRLSKEVLF TEEDVKFYLA 190 200 210 220 230 240 ELALALDHLH QLGIVYRDLK PENILLDEIG HIKLTDFGLS KESVDQEKKA YSFCGTVEYM 250 260 270 280 290 300 APEVVNRRGH SQSADWWSYG VLMFEMLTGT LPFQGKDRNE TMNMILKAKL GMPQFLSAEA 310 320 330 340 350 360 QSLLRMLFKR NPANRLGSEG VEEIKRHLFF ANIDWDKLYK REVQPPFKPA SGKPDDTFCF 370 380 390 400 410 420 DPEFTAKTPK DSPGLPASAN AHQLFKGFSF VATSIAEEYK ITPITSANVL PIVQINGNAA 430 440 450 460 470 480 QFGEVYELKE DIGVGSYSVC KRCIHATTNM EFAVKIIDKS KRDPSEEIEI LMRYGQHPNI 490 500 510 520 530 540 ITLKDVFDDG RYVYLVTDLM KGGELLDRIL KQKCFSEREA SDILYVISKT VDYLHCQGVV 550 560 570 580 590 600 HRDLKPSNIL YMDESASADS IRICDFGFAK QLRGENGLLL TPCYTANFVA PEVLMQQGYD 610 620 630 640 650 660 AACDIWSLGV LFYTMLAGYT PFANGPNDTP EEILLRIGNG KFSLSGGNWD NISDGAKDLL 670 680 690 700 710 720 SHMLHMDPHQ RYTAEQILKH SWITHRDQLP NDQPKRNDVS HVVKGAMVAT YSALTHKTFQ 730 740 PVLEPVAASS LAQRRSMKKR TSTGL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"A novel ribosomal S6-kinase (RSK4; RPS6KA6) is commonly deleted in patients with complex X-linked mental retardation." Yntema H.G., van den Helm B., Kissing J., van Duijnhoven G., Poppelaars F., Chelly J., Moraine C., Fryns J.-P., Hamel B.C.J., Heilbronner H., Pander H.-J., Brunner H.G., Ropers H.-H., Cremers F.P.M., van Bokhoven H. Genomics 62:332-343(1999) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[4]	"The DNA sequence of the human X chromosome." Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C. , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R. Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"A large-scale RNAi screen in human cells identifies new components of the p53 pathway." Berns K., Hijmans E.M., Mullenders J., Brummelkamp T.R., Velds A., Heimerikx M., Kerkhoven R.M., Madiredjo M., Nijkamp W., Weigelt B., Agami R., Ge W., Cavet G., Linsley P.S., Beijersbergen R.L., Bernards R. Nature 428:431-437(2004) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION IN P53/TP53 SIGNALING.
[7]	"Functional characterization of human RSK4, a new 90-kDa ribosomal S6 kinase, reveals constitutive activation in most cell types." Duemmler B.A., Hauge C., Silber J., Yntema H.G., Kruse L.S., Kofoed B., Hemmings B.A., Alessi D.R., Froedin M. J. Biol. Chem. 280:13304-13314(2005) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, ENZYME REGULATION, INTERACTION WITH MAPK3, SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-232; SER-372; SER-389 AND THR-581, MUTAGENESIS OF SER-372; SER-389 AND THR-581.
[8]	"The RSK family of kinases: emerging roles in cellular signalling." Anjum R., Blenis J. Nat. Rev. Mol. Cell Biol. 9:747-758(2008) [PubMed] [Europe PMC] [Abstract] Cited for: REVIEW ON FUNCTION.
[9]	"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-389, MASS SPECTROMETRY.
[10]	"Patterns of somatic mutation in human cancer genomes." Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R. Nature 446:153-158(2007) [PubMed] [Europe PMC] [Abstract] Cited for: VARIANTS [LARGE SCALE ANALYSIS] CYS-140; THR-258 AND ASN-692.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF184965 mRNA. Translation: AAF13190.1. CR536566 mRNA. Translation: CAG38803.1. AK313240 mRNA. Translation: BAG36051.1. AL389887, AL354653 Genomic DNA. Translation: CAC16111.2. AL354653, AL389887 Genomic DNA. Translation: CAD13486.2. CH471104 Genomic DNA. Translation: EAW98575.1.
IPI	IPI00007123.
RefSeq	NP_055311.1. NM_014496.4.
UniGene	Hs.234478.
3D structure databases
ProteinModelPortal	Q9UK32.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9UK32. 2 interactions.
MINT	MINT-1424416.
STRING	9606.ENSP00000262752.
PTM databases
PhosphoSite	Q9UK32.
Polymorphism databases
DMDM	11133131.
Proteomic databases
PaxDb	Q9UK32.
PRIDE	Q9UK32.
Protocols and materials databases
DNASU	27330.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000262752; ENSP00000262752; ENSG00000072133.
GeneID	27330.
KEGG	hsa:27330.
UCSC	uc004eej.2. human.
Organism-specific databases
CTD	27330.
GeneCards	GC0XM083318.
HGNC	HGNC:10435. RPS6KA6.
HPA	HPA002852. HPA003904.
MIM	300303. gene.
neXtProt	NX_Q9UK32.
PharmGKB	PA34850.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000233033.
HOVERGEN	HBG108317.
InParanoid	Q9UK32.
KO	K04373.
OrthoDB	EOG4N30N9.
PhylomeDB	Q9UK32.
Enzyme and pathway databases
BRENDA	2.7.11.1. 2681.
Reactome	REACT_111045. Developmental Biology. REACT_13685. Neuronal System.
Gene expression databases
ArrayExpress	Q9UK32.
Bgee	Q9UK32.
CleanEx	HS_RPS6KA6.
Genevestigator	Q9UK32.
GermOnline	ENSG00000072133. Homo sapiens.
Family and domain databases
InterPro	IPR000961. AGC-kinase_C. IPR011009. Kinase-like_dom. IPR017892. Pkinase_C. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR016239. Ribosomal_S6_kinase_II. IPR002290. Ser/Thr_dual-sp_kinase_dom. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 2 hits. PF00433. Pkinase_C. 1 hit. [Graphical view]
PIRSF	PIRSF000606. Ribsml_S6_kin_2. 1 hit.
SMART	SM00133. S_TK_X. 1 hit. SM00220. S_TKc. 2 hits. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 2 hits.
PROSITE	PS51285. AGC_KINASE_CTER. 1 hit. PS00107. PROTEIN_KINASE_ATP. 2 hits. PS50011. PROTEIN_KINASE_DOM. 2 hits. PS00108. PROTEIN_KINASE_ST. 2 hits. [Graphical view]
ProtoNet	Search...
Other
BindingDB	Q9UK32.
ChEMBL	CHEMBL4924.
GenomeRNAi	27330.
NextBio	50372.
SOURCE	Search...

Entry information

Entry name

KS6A6_HUMAN

Accession

Primary (citable) accession number: Q9UK32
Secondary accession number(s): B2R854 , Q6FHX2, Q8WX28, Q9H4S6

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 1, 2000
Last sequence update:	May 1, 2000
Last modified:	May 1, 2013
This is version 118 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.